Tripeptidyl peptidases: enzymes that count.

Abstract

Protein degradation is essential for the life and death of every cell. Proteins are broken down to their constitutive amino acids by a succession of peptidases, both in lysosomes and in the cytosol. Tripeptidyl-peptidases I and II are enzymes that can 'count to three' and release N-terminal tripeptides from oligopeptides generated by different endopeptidases. The tripeptides are then degraded by other exopeptidases to release amino acids and dipeptides. Mutations in tripeptidyl-peptidase I have recently been associated with a lysosomal storage disease, late infantile neuronal ceroid lipofuscinosis.

• Authors: B Tomkinson
• Journal: Trends in biochemical sciences (Trends Biochem Sci) Vol. 24 Issue 9 Pg. 355-9 (Sep 1999) ISSN: 0968-0004 [Print] England
• PMID: 10470035 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Multienzyme Complexes
• Peptides
• Proteins
• Tripeptidyl-Peptidase 1
• Endopeptidases
• Serine Proteases
• Aminopeptidases
• Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
• tripeptidyl-peptidase 2
• TPP1 protein, human
• Serine Endopeptidases
• Cysteine Endopeptidases
• Proteasome Endopeptidase Complex

Topics

• Aminopeptidases
• Cysteine Endopeptidases (metabolism)
• Cytosol (metabolism)
• Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
• Endopeptidases (genetics, metabolism)
• Humans
• Lysosomal Storage Diseases (metabolism)
• Lysosomes (metabolism)
• Multienzyme Complexes (metabolism)
• Neuronal Ceroid-Lipofuscinoses (metabolism)
• Peptides (metabolism)
• Proteasome Endopeptidase Complex
• Proteins (metabolism)
• Serine Endopeptidases (metabolism)
• Serine Proteases
• Tripeptidyl-Peptidase 1